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Sci. Signal., 24 May 2011
[DOI: 10.1126/scisignal.2001823]

Supplementary Materials for:

α-Catenin Is a Tumor Suppressor That Controls Cell Accumulation by Regulating the Localization and Activity of the Transcriptional Coactivator Yap1

Mark R. Silvis, Bridget T. Kreger, Wen-Hui Lien, Olga Klezovitch, G. Marianna Rudakova, Fernando D. Camargo, Dan M. Lantz, John T. Seykora, Valeri Vasioukhin*

*To whom correspondence should be addressed. E-mail: vvasiouk{at}fhcrc.org

This PDF file includes:

  • Fig. S1. Generation of GFAP-Cre/αE-cateninfl/fl mice.
  • Fig. S2. Skin histology of GFAP-Cre/αE-cateninfl/fl mice.
  • Fig. S3. Increased rates of cell proliferation in αE-catenin−/− stem and early progenitor cells.
  • Fig. S4. Inflammatory response in hair follicle cysts and tumors from mice with conditional knockout of αE-catenin or of αE-catenin and p53.
  • Fig. S5. Tumors in GFAP-Cre/αE-cateninfl/fl mice are derived from αE-catenin−/− keratinocytes.
  • Fig. S6. Apoptosis in hair follicle cysts from mice with conditional knockout of αE-catenin or of αE-catenin and p53.
  • Fig. S7. αE-catenin is necessary for contact-mediated inhibition of cell accumulation.
  • Fig. S8. Ninety-six–well plate assay for contact inhibition of cell accumulation.
  • Fig. S9. Efficient knockdown of gene targets after siRNA transfection in 96-well plate contact inhibition assay.
  • Fig. S10. siRNA screen for genes required for αE-catenin–mediated contact inhibition.
  • Fig. S11. Efficient knockdown of Yap1 after transfection of keratinocytes with siRNA oligos.
  • Fig. S12. Nuclear localization of Yap1 in subconfluent αE-cateninfl/fl and αE-catenin−/− keratinocytes.
  • Fig. S13. Increased nuclear localization of Yap1 in confluent αE-catenin−/− keratinocytes.
  • Fig. S14. Rescue of cytoplasmic localization of Yap1 in αE-catenin−/− cells transduced with retroviruses expressing full-length αE-catenin.
  • Fig. S15. Partial colocalization between αE-catenin and Yap1 in confluent keratinocytes.
  • Fig. S16. Yap1 is nuclear in both dividing and nondividing subconfluent keratinocytes.
  • Fig. S17. Western blot analysis of Hippo pathway proteins in cultured keratinocytes.
  • Fig. S18. Quantitation of Yap1-specific phosphorylation on Ser127.
  • Fig. S19. Decreased abundance of Yap1 mRNA in αE-catenin−/− keratinocytes.
  • Fig. S20. Acute knockdown of αE-catenin reduces total Yap1 protein abundance.
  • Fig. S21. Nuclear localization of Yap1 in αE-catenin−/− cortical neural progenitor cells.
  • Fig. S22. Hippo pathway siRNA screen on cultured αE-cateninfl/fl (Ctrl) and αE-catenin−/− (α-cat−/−) keratinocytes.
  • Fig. S23. Wild-type, but not S94A mutant, human Yap2 protein is necessary for increased cell proliferation in αE-catenin−/− keratinocytes.
  • Fig. S24. qRT-PCR analysis of Cyr61 expression in 4-month-old skin and tumors from αE-cateninfl/fl (Ctrl) and GFAP-Cre/αE-cateninfl/fl (α-cat cKO) mice.
  • References

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Citation: M. R. Silvis, B. T. Kreger, W.-H. Lien, O. Klezovitch, G. M. Rudakova, F. D. Camargo, D. M. Lantz, J. T. Seykora, V. Vasioukhin, α-Catenin Is a Tumor Suppressor That Controls Cell Accumulation by Regulating the Localization and Activity of the Transcriptional Coactivator Yap1. Sci. Signal. 4, ra33 (2011).

© 2011 American Association for the Advancement of Science


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